ID A0A1J0VBW6_9GAMM Unreviewed; 363 AA. AC A0A1J0VBW6; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 25-MAY-2022, entry version 20. DE RecName: Full=Bifunctional chorismate mutase/prephenate dehydratase {ECO:0000256|ARBA:ARBA00014401}; DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147}; DE EC=5.4.99.5 {ECO:0000256|ARBA:ARBA00012404}; DE AltName: Full=Chorismate mutase-prephenate dehydratase {ECO:0000256|ARBA:ARBA00031520}; DE AltName: Full=p-protein {ECO:0000256|ARBA:ARBA00031175}; GN ORFNames=BOX17_00255 {ECO:0000313|EMBL:APE29526.1}; OS Halomonas aestuarii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=1897729 {ECO:0000313|EMBL:APE29526.1, ECO:0000313|Proteomes:UP000181985}; RN [1] {ECO:0000313|Proteomes:UP000181985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hb3 {ECO:0000313|Proteomes:UP000181985}; RA Koh H.-W., Rani S., Park S.-J.; RT "Halolamina sediminis sp. nov., an extremely halophilic archaeon isolated RT from solar salt."; RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to CC prephenate and the decarboxylation/dehydration of prephenate to CC phenylpyruvate. {ECO:0000256|ARBA:ARBA00002364}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O; CC Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51; CC Evidence={ECO:0000256|ARBA:ARBA00000913}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; CC Evidence={ECO:0000256|ARBA:ARBA00000824}; CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; CC phenylpyruvate from prephenate: step 1/1. CC {ECO:0000256|ARBA:ARBA00004741}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis; CC prephenate from chorismate: step 1/1. {ECO:0000256|ARBA:ARBA00004817}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP018139; APE29526.1; -; Genomic_DNA. DR RefSeq; WP_071941509.1; NZ_CP018139.1. DR EnsemblBacteria; APE29526; APE29526; BOX17_00255. DR KEGG; hsi:BOX17_00255; -. DR UniPathway; UPA00120; UER00203. DR UniPathway; UPA00121; UER00345. DR Proteomes; UP000181985; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC. DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro. DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.59.10; -; 1. DR InterPro; IPR045865; ACT-like_dom_sf. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR008242; Chor_mutase/pphenate_deHydtase. DR InterPro; IPR036263; Chorismate_II_sf. DR InterPro; IPR036979; CM_dom_sf. DR InterPro; IPR002701; CM_II_prokaryot. DR InterPro; IPR010957; G/b/e-P-prot_chorismate_mutase. DR InterPro; IPR001086; Preph_deHydtase. DR InterPro; IPR018528; Preph_deHydtase_CS. DR Pfam; PF01842; ACT; 1. DR Pfam; PF01817; CM_2; 1. DR Pfam; PF00800; PDT; 1. DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1. DR SMART; SM00830; CM_2; 1. DR SUPFAM; SSF48600; SSF48600; 1. DR SUPFAM; SSF55021; SSF55021; 1. DR TIGRFAMs; TIGR01807; CM_P2; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS51168; CHORISMATE_MUT_2; 1. DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1. DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1. DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1. PE 4: Predicted; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}; KW Reference proteome {ECO:0000313|Proteomes:UP000181985}. FT DOMAIN 2..94 FT /note="Chorismate mutase" FT /evidence="ECO:0000259|PROSITE:PS51168" FT DOMAIN 94..270 FT /note="Prephenate dehydratase" FT /evidence="ECO:0000259|PROSITE:PS51171" FT DOMAIN 282..359 FT /note="ACT" FT /evidence="ECO:0000259|PROSITE:PS51671" FT COILED 8..28 FT /evidence="ECO:0000256|SAM:Coils" FT SITE 263 FT /note="Essential for prephenate dehydratase activity" FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2" SQ SEQUENCE 363 AA; 40548 MW; 17D9F372D71D33B1 CRC64; MTEPSVSLEA LRQRIDALDN DILRLISERA ACAQEVAAIK AEHEPGGVFY RPEREAQVLR RVMELNHGPL DSEEMARLFR EIMSACLALE QPVKVAYLGP EGTFTQQAAL KHFGESAISL PMAAIDEVFR EVEAGAVNYG VVPVENSTEG VINHTLDSFM DSSLRICGEV VLRIHHHLLV SETTRRDKVS RIYSHPQSFA QCRKWIDAHF PQAERVPVSS NAEAARLVKT EWHSAAIAGD MAAKLYGLAR LAEKIEDRPD NSTRFLIIGN QDVPVSGEDK TSLVVAMRNQ PGALHDLLEP FHRHQIDMTR LETRPSRSGV WNYVFFIDFK GHRDEPRVAA MLEEVKLRAA DVKVLGSYPA GVL //